A6380
α-Amylase from Bacillus sp.
Type II-A, lyophilized powder, ≥1,500 units/mg protein (biuret)
Sign Into View Organizational & Contract Pricing
All Photos(4)
Recommended Products
biological source
bacterial (Bacillus amyloliquefaciens)
Quality Level
type
Type II-A
Assay
≥30%
form
lyophilized powder
specific activity
≥1,500 units/mg protein (biuret)
mol wt
50-55 kDa by SDS-PAGE
technique(s)
SDS-PAGE: suitable
solubility
H2O: soluble 0.1 mg/mL, clear, colorless
suitability
suitable for hydrolysis, synthesis of oligosaccharides and polysaccharides, and sugar modification
application(s)
life science and biopharma
storage temp.
−20°C
Looking for similar products? Visit Product Comparison Guide
Related Categories
General description
α-Amylase (1,4-α-d-glucan glucohydrolase), an endo-acting glucanase, is a member of the glycoside hydrolase family 13 (GH13).
α-Amylase, an extracellular enzyme, is present in many animals and plants, and also in microorganisms, such as different Bacillus species.
Application
α-Amylase from Bacillus sp. has been used:
- as a component of salivary fluid to perform artificial mastication; in luminal gastrointestinal digestion experiment
- as a standard in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to determine the concentration of α-Amylase
- to de-starch the alcohol insoluble residue (AIR) for non-cellulosic neutral monosaccharide analysis
Biochem/physiol Actions
α-Amylase degrades starch into oligosaccharides such as maltose, and glucose and alpha limit dextrin. It hydrolyzes the α-(1→4) glucosidic linkages in polysaccharides of three or more α-(1→4) linked D-glucose units, without hydrolyzing the α-(1→6) bond. It participates in glucose production and is essential for energy acquisition. α-Amylases are widely known industrial enzymes used in the food, detergent, textile, fermentation, and pharmaceutical industries.
Features and Benefits
- α-Amylase from Bacillus licheniformis NCIB 6346 retains over 98% of its activity after 60 minutes at pH 6.2 and 85°C.
- Other α-Amylase maintain 100% of their activity after storage for 1 hour at 91°C.
Maintains >98% of activity after 60 minutes at pH 6.2 at 85 °C.
Unit Definition
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
Preparation Note
4× crystallized
Dissolves in water to form a clear, colorless solution at 0.1 mg/mL concentration.
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
This product is for R&D use only, not for drug, household, or other uses. Please consult the Safety Data Sheet for information regarding hazards and safe handling practices.
substrate
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Andrzej T Lulko et al.
Applied and environmental microbiology, 73(16), 5354-5362 (2007-06-26)
Transcriptome analysis was used to investigate the global stress response of the gram-positive bacterium Bacillus subtilis caused by overproduction of the well-secreted AmyQ alpha-amylase from Bacillus amyloliquefaciens. Analyses of the control and overproducing strains were carried out at the end
Immobilized Enzymes on Gold Nanoparticles: From Enhanced Stability to Cleaning of Heritage Textiles.
Francesca Gherardi et al.
ACS applied bio materials, 2(11), 5136-5143 (2019-11-18)
Enzyme-based treatments are used in heritage conservation for the effective removal of glues and other damaging organic layers from the surfaces of historic and artistic works. Despite their potential, however, the application of enzymatic treatments is currently limited because of
Vincent T Calabrese et al.
Biotechnology progress, 32(5), 1271-1275 (2016-10-23)
A number of years ago we reported a two-step inactivation mechanism for α-amylase (enzyme) on the basis of theoretical and experimental studies in aqueous solutions. In the first step the metal (Ca2+ ) ion dissociates reversibly from the enzyme followed
Sun-Li Chong et al.
Analytical and bioanalytical chemistry, 401(9), 2995-3009 (2011-09-10)
The atmospheric pressure matrix-assisted laser desorption/ionization with ion trap mass spectrometry (AP-MALDI-ITMS) was investigated for its ability to analyse plant-derived oligosaccharides. The AP-MALDI-ITMS was able to detect xylooligosaccharides (XOS) with chain length of up to ten xylopyranosyl residues. Though the
Magdalena Eder et al.
Journal of phycology, 44(5), 1221-1234 (2008-10-01)
The cell wall of the green alga Micrasterias denticulata Bréb. ex Ralfs (Desmidiaceae, Zygnematophyceae, Streptophyta) was investigated to obtain information on the composition of component polysaccharides and proteoglycans to allow comparison with higher plants and to understand cell wall functions
Protocols
Follow our procedure for the determination of alpha-Amylase activity. This enzymatic assay of a-Amylase guides you through the entire process and necessary calculations.
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service